Isolation and characterization of a structurally unique β-hairpin venom peptide from the predatory ant Anochetus emarginatus

Touchard, Axel, Brust, Andreas, Cardoso, Fernanda C., Chin, K.-Y., Herzig, Volker, Jin, Ai-Hua, Dejean, Alain, Alewood, Paul F., King, Glenn F., Orivel, Jérôme and Escoubas, Pierre (2016) Isolation and characterization of a structurally unique β-hairpin venom peptide from the predatory ant Anochetus emarginatus. Biochimica et Biophysica Acta, 1860 11 Part A: 2553-2562. doi:10.1016/j.bbagen.2016.07.027

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Author Touchard, Axel
Brust, Andreas
Cardoso, Fernanda C.
Chin, K.-Y.
Herzig, Volker
Jin, Ai-Hua
Dejean, Alain
Alewood, Paul F.
King, Glenn F.
Orivel, Jérôme
Escoubas, Pierre
Title Isolation and characterization of a structurally unique β-hairpin venom peptide from the predatory ant Anochetus emarginatus
Formatted title
Isolation and characterization of a structurally unique β-hairpin venom peptide from the predatory ant Anochetus emarginatus
Journal name Biochimica et Biophysica Acta   Check publisher's open access policy
ISSN 0006-3002
Publication date 2016-07-28
Sub-type Article (original research)
DOI 10.1016/j.bbagen.2016.07.027
Open Access Status File (Author Post-print)
Volume 1860
Issue 11 Part A
Start page 2553
End page 2562
Total pages 10
Place of publication Amsterdam, Netherlands
Publisher Elsevier
Language eng
Formatted abstract
Background

Most ant venoms consist predominantly of small linear peptides, although some contain disulfide-linked peptides as minor components. However, in striking contrast to other ant species, some Anochetus venoms are composed primarily of disulfide-rich peptides. In this study, we investigated the venom of the ant Anochetus emarginatus with the aim of exploring these novel disulfide-rich peptides.

Methods

The venom peptidome was initially investigated using a combination of reversed-phase HPLC and mass spectrometry, then the amino acid sequences of the major peptides were determined using a combination of Edman degradation and de novo MS/MS sequencing. We focused on one of these peptides, U1-PONTX-Ae1a (Ae1a), because of its novel sequence, which we predicted would form a novel 3D fold. Ae1a was chemically synthesized using Fmoc chemistry and its 3D structure was elucidated using NMR spectroscopy. The peptide was then tested for insecticidal activity and its effect on a range of human ion channels.

Results

Seven peptides named poneritoxins (PONTXs) were isolated and sequenced. The three-dimensional structure of synthetic Ae1a revealed a novel, compact scaffold in which a C-terminal β-hairpin is connected to the N-terminal region via two disulfide bonds. Synthetic Ae1a reversibly paralyzed blowflies and inhibited human L-type voltage-gated calcium channels (CaV1).

Conclusions

Poneritoxins from Anochetus emarginatus venom are a novel class of toxins that are structurally unique among animal venoms.

General significance

This study demonstrates that Anochetus ant venoms are a rich source of novel ion channel modulating peptides, some of which might be useful leads for the development of biopesticides.
Keyword Ant venom
Anochetus
Poneritoxins
U1-PONTX-Ae1a
Disulfide-rich peptides
Neurotoxin
L-type calcium channels
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: HERDC Pre-Audit
Institute for Molecular Bioscience - Publications
 
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Created: Fri, 02 Sep 2016, 23:20:17 EST by Fernanda Caldas Cardoso on behalf of Institute for Molecular Bioscience